Biophysical characterization of ORF104 in Streptococcus sanguinis: Helical wheel and amphipathicity analysis

This dataset contains the biophysical validation of the ORF104 peptide (50 aa) identified in the Streptococcus sanguinis genome. Through a sliding window analysis (18 aa) using the HeliQuest algorithm, we identified key structural regions: Maximum Hydrophobicity: A peak value of 1.105 (residues 15-32), confirming a robust transmembrane core. Maximum Amphipathicity: A hydrophobic moment (μH) of 0.413 (residues 9-26), indicating a high potential for protein-protein or protein-lipid interactions. Hydrophobic Face: Identification of a clear non-polar face (A I L V L M C I) consistent with the structural architecture of the Oblin protein family. These findings complement the AlphaFold 3 structural models and support the classification of ORF104 as a membrane-associated protein